Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
H115W | significant decrease in the rate of catalysis, moderate increase of the affinity of the substrate | Homo sapiens |
H115W/R192K | kinetic parameters comparable to mutant H115W | Homo sapiens |
H115W/R192Q | complete loss of activity | Homo sapiens |
additional information | the presence of a (His)6-tag at the N-terminus and at both the N- and C-termini decreases the enzymatic activity of the recombinant protein. The activity is unaffected by the presence of a (His)6-tag at its C-terminus | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.4 | - |
delta-valerolactone | mutant H115W, pH 8.3, 25°C | Homo sapiens | |
0.5 | - |
delta-valerolactone | mutant H115W/R192K, pH 8.3, 25°C | Homo sapiens | |
1.5 | - |
delta-valerolactone | wild-type, pH 8.3, 25°C | Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
40000 | - |
x * 40000, SDS-PAGE | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P27169 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
delta-valerolactone + H2O | - |
Homo sapiens | 5-hydroxypentanoic acid | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 40000, SDS-PAGE | Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.5 | - |
delta-valerolactone | mutant H115W, pH 8.3, 25°C | Homo sapiens | |
0.9 | - |
delta-valerolactone | mutant H115W/R192K, pH 8.3, 25°C | Homo sapiens | |
29.8 | - |
delta-valerolactone | wild-type, pH 8.3, 25°C | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | the presence of a particular amino acid residue at position 192 differentially alters the effect of the H115W substitution, and the H115 residue is not always needed for the lactonase and arylesterase activities of the enzyme. The amino acid residues at position 192 and 115 act in conjunction in modulating the hydrolytic activities of the enzyme | Homo sapiens |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.3 | - |
delta-valerolactone | mutant H115W, pH 8.3, 25°C | Homo sapiens | |
1.9 | - |
delta-valerolactone | mutant H115W/R192K, pH 8.3, 25°C | Homo sapiens | |
19.8 | - |
delta-valerolactone | wild-type, pH 8.3, 25°C | Homo sapiens |